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Entry: A0A235F6S5_9BACI
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ID   A0A235F6S5_9BACI        Unreviewed;       957 AA.
AC   A0A235F6S5;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=UvrABC system protein A {ECO:0000256|ARBA:ARBA00039316, ECO:0000256|HAMAP-Rule:MF_00205};
DE            Short=UvrA protein {ECO:0000256|HAMAP-Rule:MF_00205};
DE   AltName: Full=Excinuclease ABC subunit A {ECO:0000256|ARBA:ARBA00042156, ECO:0000256|HAMAP-Rule:MF_00205};
GN   Name=uvrA {ECO:0000256|HAMAP-Rule:MF_00205};
GN   ORFNames=CGZ90_14680 {ECO:0000313|EMBL:OYD56952.1};
OS   Fictibacillus aquaticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX   NCBI_TaxID=2021314 {ECO:0000313|EMBL:OYD56952.1, ECO:0000313|Proteomes:UP000215059};
RN   [1] {ECO:0000313|EMBL:OYD56952.1, ECO:0000313|Proteomes:UP000215059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GDSW-R2A3 {ECO:0000313|EMBL:OYD56952.1,
RC   ECO:0000313|Proteomes:UP000215059};
RA   Mayilraj S.;
RT   "Fictibacillus sp. nov. GDSW-R2A3 Genome sequencing and assembly.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The UvrABC repair system catalyzes the recognition and
CC       processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein.
CC       A damage recognition complex composed of 2 UvrA and 2 UvrB subunits
CC       scans DNA for abnormalities. When the presence of a lesion has been
CC       verified by UvrB, the UvrA molecules dissociate. {ECO:0000256|HAMAP-
CC       Rule:MF_00205}.
CC   -!- SUBUNIT: Forms a heterotetramer with UvrB during the search for
CC       lesions. {ECO:0000256|HAMAP-Rule:MF_00205}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00205}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. UvrA family.
CC       {ECO:0000256|ARBA:ARBA00038000, ECO:0000256|HAMAP-Rule:MF_00205}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OYD56952.1}.
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DR   EMBL; NOII01000008; OYD56952.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A235F6S5; -.
DR   OrthoDB; 9809851at2; -.
DR   Proteomes; UP000215059; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR   CDD; cd03270; ABC_UvrA_I; 1.
DR   CDD; cd03271; ABC_UvrA_II; 1.
DR   Gene3D; 1.10.8.280; ABC transporter ATPase domain-like; 1.
DR   Gene3D; 1.20.1580.10; ABC transporter ATPase like domain; 2.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   HAMAP; MF_00205; UvrA; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004602; UvrA.
DR   InterPro; IPR041552; UvrA_DNA-bd.
DR   InterPro; IPR041102; UvrA_inter.
DR   NCBIfam; TIGR00630; uvra; 1.
DR   PANTHER; PTHR43152; UVRABC SYSTEM PROTEIN A; 1.
DR   PANTHER; PTHR43152:SF3; UVRABC SYSTEM PROTEIN A; 1.
DR   Pfam; PF17755; UvrA_DNA-bind; 1.
DR   Pfam; PF17760; UvrA_inter; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00205};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   DNA excision {ECO:0000256|ARBA:ARBA00022769, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   Excision nuclease {ECO:0000256|ARBA:ARBA00022881, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00205}; Reference proteome {ECO:0000313|Proteomes:UP000215059};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00205};
KW   SOS response {ECO:0000256|ARBA:ARBA00023236, ECO:0000256|HAMAP-
KW   Rule:MF_00205};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00205};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW   Rule:MF_00205}.
FT   DOMAIN          605..936
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   ZN_FING         253..280
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   ZN_FING         739..765
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         34..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
FT   BINDING         640..647
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00205"
SQ   SEQUENCE   957 AA;  106397 MW;  E8316AD06ACAD38C CRC64;
     MAANQNLTVK GARAHNLKNI DVTIPRDKLV VLTGLSGSGK SSLAFDTIYA EGQRRYVESL
     SAYARQFLGQ MDKPDVDSIE GLSPAISIDQ KTTSRNPRST VGTVTEIYDY LRLLFARIGR
     PVCPTHGVEI TSQTIEQMVD RIIEYPERTK LQILAPVVSG RKGEHVKVLE DIKKQGYVRV
     RIDGEMREIS EEISLEKNKK HSIEVVVDRI VIKEGIMTRL SDSLETALNL AEGSVIVDVM
     GEEELLFSQN HACPYCGFSI GELEPRLFSF NSPFGACQSC DGLGVKLEVD PELVIPDWSR
     SLKDHAIAPW EPVSSQYYPQ LLESIATHFG IDMEVPVEDL PKDQMDKILN GSSKDRILFT
     YRNDFGQVRK NEIIFEGVLS NIERRYRETS SDYIREQMEG YMAQKPCPKC KGHRLKKEAL
     SVLINGKHIG ETTQMSITEA NKFFNNLELT EKEQAIAKLI LREIVDRSGF LINVGLDYLT
     FSRAAGTLSG GEAQRIRLAT QVGSRLMGVL YILDEPSIGL HQRDNDRLIR TLEEMRSLGN
     TLIVVEHDED TMFAADYIID IGPGAGAHGG TITAQGTPQE IMEDPNSLTG QYLSGKKFIP
     LPSERRKPDG RYIEVLGMSE NNLKNANVKI PLGVFTGVTG VSGSGKSTFV NEILHKALAQ
     KLHRAKDKPG AHKAIKGLDH VDKVIDIDQS PIGRTPRSNP ATYTGVFDDI RDVFASTNEA
     KVRGYKKGRF SFNVKGGRCE ACRGDGIIKI EMHFLPDVYV PCEICHGKRY NRETLEVKYK
     GKSIADILDM TVEESVDFFA NIPKIRRKME TILDVGLGYI KLGQSATTLS GGEAQRVKLA
     SQLHKRSTGK TIYILDEPTT GLHVDDISRL LKVLQRIVDN GDSVLVIEHN LDVIKQCDHL
     IDMGPEGGDK GGTVVGTGTP EELAKVEASH TGRYLAPILK RDKKRMSKIM KEKETVK
//
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